Glutathionylation of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the model plant Arabidopsis thaliana is reversed by both glutaredoxins and thioredoxins in vitro (Record no. 50974)

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fixed length control field 02683nam a2200325Ia 4500
003 - CONTROL NUMBER IDENTIFIER
control field MX-MdCICY
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20250625160158.0
040 ## - CATALOGING SOURCE
Transcribing agency CICY
090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN)
Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) B-16809
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245 10 - TITLE STATEMENT
Title Glutathionylation of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the model plant Arabidopsis thaliana is reversed by both glutaredoxins and thioredoxins in vitro
490 0# - SERIES STATEMENT
Volume/sequential designation BioChemical Journal, 445(3), p.337-347, 2012
520 3# - SUMMARY, ETC.
Summary, etc. Plants contain both cytosolic and chloroplastic GAPDHs (glyceraldehyde-3- phosphate dehydrogenases). In Arabidopsis thaliana, cytosolic GAPDH is involved in the glycolytic pathway and is represented by two differentially expressed isoforms (GapC1 and GapC2)that are 98 percent identical in amino acid sequence. In the present study we show that GapC1 is a phosphorylating NAD-specific GAPDH with enzymatic activity strictly dependent on Cys149. Catalytic Cys 149 is the only solvent-exposed cysteine of the protein and its thiol is relatively acidic (pKa = 5.7). This property makes GapC1 sensitive to oxidation by H2O2, which appears to inhibit enzyme activity by converting the thiolate of Cys149 (-S-)into irreversible oxidized forms (-SO2 - and -SO 3 -)via a labile sulfenate intermediate (-SO-). GSH (reduced glutathione)prevents this irreversible process by reacting with Cys149 sulfenates to give rise to a mixed disulfide (Cys 149-SSG), as demonstrated by both MS and biotinylated GSH. Glutathionylated GapC1 can be fully reactivated either by cytosolic glutaredoxin, via a GSH-dependent monothiol mechanism, or, less efficiently, by cytosolic thioredoxins physiologically reduced by NADPH:thioredoxin reductase. The potential relevance of these findings is discussed in the light of the multiple functions of GAPDH in eukaryotic cells (e.g. glycolysis, control of gene expression and apoptosis)that appear to be influenced by the redox state of the catalytic Cys149. © The Authors Journal compilation
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element ARABIDOPSIS THALIANA CYTOSOLIC ISOFORM 1 GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE (ATGAPC1)
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element DEGLUTATHIONYLATION
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element GLUTATHIONYLATION
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element GLYCOLYSIS
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element OXIDATIVE STRESS
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element REDOX SIGNALLING
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Bedhomme, M.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Adamo, M.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Marchand, C.H.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Couturier, J.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Rouhier, N.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Lemaire, S.D.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Zaffagnini, M.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Zaffagnini, M.
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier <a href="https://drive.google.com/file/d/1xuZHXcSFA53GokKDyAx73eq6y_W474zJ/view?usp=drivesdk">https://drive.google.com/file/d/1xuZHXcSFA53GokKDyAx73eq6y_W474zJ/view?usp=drivesdk</a>
Public note Para ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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Source of classification or shelving scheme Clasificación local
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  Clasificación local     Ref1 CICY CICY Documento préstamo interbibliotecario 25.06.2025   B-16809 25.06.2025 25.06.2025 Documentos solicitados